|
type |
Journal Article |
authors |
Grimm, B.; Bull, A.; Welinder, K. G.; Gough, S. P.; Kannangara, C. G. |
title |
Purification and partial amino acid sequence of the glutamate 1- semialdehyde aminotransferase of barley and synechococcus |
journal |
Carlsberg Res Commun |
Activity |
5.4.3.8 |
Family |
5.4.3.8 |
ui |
89374545 |
year |
(1989) |
volume |
54 |
number |
2 |
pages |
67-79 |
| |
keywords |
Amino Acid Sequence |
abstract |
Glutamate-1-semialdehyde aminotransferase (E.C. 5.4.3.8) was purified from barley and the cyanobacteria Synechococcus PCC 6301. The purification procedure involved serial affinity chromatography and preparative polyacrylamide gel electrophoresis under non-denaturing conditions. The aminotransferase of these two organisms showed different mobilities in non-denaturing gels. In SDS-PAGE the enzyme from both organisms migrated as a single protein with an apparent molecular weight of 46.000 Da. An antibody against the barley enzyme cross-reacted with the cyanobacterial aminotransferase. This antibody also recognized a 17 kDa peptide cleaved from the barley protein with cyanogen bromide. Amino acid sequences of the NH2-termini revealed significant homology between the eucaryotic and cyanobacterial enzyme. |
last changed |
2008/05/21 16:26 |
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